ID A0A2N1JQB8_9BACI Unreviewed; 390 AA. AC A0A2N1JQB8; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 05-DEC-2018, entry version 4. DE RecName: Full=Chorismate synthase {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605}; DE Short=CS {ECO:0000256|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300}; GN ORFNames=CWE34_29585 {ECO:0000313|EMBL:PKJ52125.1}; OS Bacillus sp. SN10. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2056493 {ECO:0000313|EMBL:PKJ52125.1, ECO:0000313|Proteomes:UP000233528}; RN [1] {ECO:0000313|EMBL:PKJ52125.1, ECO:0000313|Proteomes:UP000233528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SN10 {ECO:0000313|EMBL:PKJ52125.1, RC ECO:0000313|Proteomes:UP000233528}; RA Nazipi S.; RT "Bacillus sp. isolated from nest material of social spiders."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate CC and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate CC (EPSP) to yield chorismate, which is the branch point compound CC that serves as the starting substrate for the three terminal CC pathways of aromatic amino acid biosynthesis. This reaction CC introduces a second double bond into the aromatic ring system. CC {ECO:0000256|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}; CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00300, ECO:0000256|RuleBase:RU000605}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 7/7. {ECO:0000256|HAMAP-Rule:MF_00300, CC ECO:0000256|RuleBase:RU000605}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PKJ52125.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PJCU01000029; PKJ52125.1; -; Genomic_DNA. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000233528; Unassembled WGS sequence. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd07304; Chorismate_synthase; 1. DR Gene3D; 3.60.150.10; -; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR035904; Chorismate_synth_AroC_sf. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; PTHR21085; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; SSF103263; 1. DR TIGRFAMs; TIGR00033; aroC; 1. DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1. DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1. DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00300, KW ECO:0000256|RuleBase:RU000605}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00300, KW ECO:0000256|RuleBase:RU000605}; KW Complete proteome {ECO:0000313|Proteomes:UP000233528}; KW FAD {ECO:0000256|HAMAP-Rule:MF_00300}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00300}; KW FMN {ECO:0000256|HAMAP-Rule:MF_00300}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00300, KW ECO:0000256|RuleBase:RU000605}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00300}. FT NP_BIND 132 134 FMN. {ECO:0000256|HAMAP-Rule:MF_00300}. FT NP_BIND 253 254 FMN. {ECO:0000256|HAMAP-Rule:MF_00300}. FT NP_BIND 313 317 FMN. {ECO:0000256|HAMAP-Rule:MF_00300}. FT BINDING 39 39 NADP. {ECO:0000256|HAMAP-Rule:MF_00300}. FT BINDING 45 45 NADP. {ECO:0000256|HAMAP-Rule:MF_00300}. FT BINDING 298 298 FMN; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00300}. FT BINDING 339 339 FMN. {ECO:0000256|HAMAP-Rule:MF_00300}. SQ SEQUENCE 390 AA; 42482 MW; B84ABCD0BFFCF55D CRC64; MRYITAGESH GPQLTVILEG VPAGLTLAAE HINKELLRRQ KGHGRGRRMQ IETDTVEIVS GVRHGMTLGS PITLIVKNDD FKHWTKVMGA EPISEKESKE MKRTITKPRP GHADLNGAIK YGHRDIRNVL ERSSARETTV RVAAGAVAKQ ILKELGVEIA GHVLEIGGVK AKHISNLSIE EIQTITENSP VRCLDKEVEQ EMMDAIDHAK SSGDSIGGIV EVIAEGMPIG VGSYVHYDRK LDAKLAGAIM SINAFKGAEI GVGFEAARQP GSKVHDEILW DEEQGYMRKT NNAGGFEGGM TTGMPIVVRG VMKPIPTLYK PLASVDIDTK EAFQASIERS DSCAVPAAGV VAESVVAWEL AHALVEQFGK DRMELIQQNI TQHNKYAKEF //